Neurochemical Research

, Volume 36, Issue 5, pp 863–869 | Cite as

Abeta Peptide Toxicity is Reduced After Treatments Decreasing Phosphatidylethanolamine Content in Differentiated Neuroblastoma Cells

  • Emanuela Cazzaniga
  • Alessandra Bulbarelli
  • Elena Lonati
  • Antonina Orlando
  • Francesca Re
  • Maria Gregori
  • Massimo Masserini
Original Paper


We investigated whether the toxicity of oligomeric amyloid-beta peptide (Abeta1-42) upon differentiated human neuroblastoma SH-SY5Y cells, can be affected by changes of membrane lipid composition. An immunostaining technique, using lipids extracted from the cells and separated by thin layer chromatography, suggested that Abeta preferentially binds to phosphatidylethanolamine (PE), one of the major lipids in the cell extract. For this reason, we utilized treatments with putative inhibitors of phosphatidylethanolamine biosynthesis (choline, phosphocholine, R59949) to decrease its proportion in the cell membrane; choline treatment (2.5 mM, 24 h) showed the best performance, reducing phosphatidylethanolamine content from 5.7 to 3.3 μg phosphorous/mg protein. Either the extent of Abeta binding or its toxicity decreased onto choline-treated cells. These data may open the possibility to develop future strategies aiming to reduce Abeta toxicity in Alzheimer disease.


Neuroblastoma SH-SY5Y Amyloid-beta peptide (1-42) Phosphatidylethanolamine Phosphatidylcholine 



Amyloid-beta peptide (1-42)







This work was supported by grants from MIUR, Italy (PRIN2005, FIRB 2003).


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Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Emanuela Cazzaniga
    • 1
  • Alessandra Bulbarelli
    • 1
  • Elena Lonati
    • 1
  • Antonina Orlando
    • 1
  • Francesca Re
    • 1
  • Maria Gregori
    • 1
  • Massimo Masserini
    • 1
  1. 1.Department of Experimental MedicineUniversity of Milano BicoccaMonzaItaly

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